• Title/Summary/Keyword: ACE-inhibitory activity

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Effect of Sodium Caseinate Hydrolysates on Angiotensin-I Converting Enzyme Inhibition Activity (Sodium Caseinate 가수분해물의 Angiotensin-I Converting Enzyme 저해효과에 관한 연구)

  • Lee, Keon-Bong;Shin, Yong-Kook;Baick, Seung-Chun
    • Food Science of Animal Resources
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    • v.32 no.5
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    • pp.652-658
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    • 2012
  • This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at $45^{\circ}C$. The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and ${\alpha}$-chymotrypsin, at $37^{\circ}C$ for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and $IC_{50}$ values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest $IC_{50}$ value ($516{\mu}g/mL$) and Flavourzyme hydrolysate showed the highest $IC_{50}$value ($866{\mu}g/mL$). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an $IC_{50}$ value ($282{\mu}g/mL$). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the $IC_{50}$ value ($597{\mu}g/mL$) was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed $273{\mu}g/mL$ of $IC_{50}$ value, showed no difference, but retentate which has over MW 10,000 showed statistically different $IC_{50}$ value, $635{\mu}g/mL$ (p<0.05).

Physiological Activity of Zizyphus jujuba Leaf Extracts (대추잎 추출물의 생리활성 작용)

  • Jin, Qing;Park, Jyung-Rewng;Kim, Jong-Bae;Cha, Myung-Hwa
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.28 no.3
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    • pp.593-598
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    • 1999
  • This study was designed to investigate the possible utilization of Zizyphus jujuba leaves as a source of functional ingredients. The physiological activity of different solvent fractions prepared from ethanol extract of Zizyphus jujuba leaves were analyzed. Xanthine oxidase inhibitory effect was very high in all fractions except chloroform fraction. The very high electron donating ability was observed in the ethylacetate fraction and the effect was similar to 0.1% tocopherol. Nitrite scavenging effect of all fractions was more than 40% even at low concentration of 1mg/ml and was increased with increasing concentration. Angiotensin I converting enzyme inhibitory activity was appeared in ethyl acetate and chloroform fractions only at high concentraton.

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Effect of Angiotensin-I Converting Enzyme Inhibitory from Hydrolysate of Soybean Protein Isolate (분리대두단백질 가수분해물의 Angiotensin-I Converting Enzyme 저해효과)

  • Back, Su-Yeon;Do, Jeong-Ryong;Do, Gun-Pyo;Kim, Hyun-Ku
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.1
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    • pp.8-13
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    • 2010
  • The angiotensin converting enzyme (ACE) inhibition effect of soybean protein isolate hydrolysate was studied using protease. Soybean protein isolate was hydrolysed by seven enzymes (Alcalase 2.4 L, Flavourzyme 500 MG, GC 106, Multifect Neutral, Neutrase 0.8 L, Papain 30,000 and Protamex), enzyme concentrations (0, 0.5, 1.0 and 1.5%), at various hydrolysis times (0, 1, 2, 3, 4, 5 and 6 hr) and suspension concentrations (1, 5, 7, 10 and 15%). Absorbance at 280 nm, brix and ACE inhibitory activity of soybean protein isolate hydrolysates were investigated. Absorbance at 280 nm and brix of Alcalase 2.4 L treatment were higher than other enzyme treatments. The optimum condition of hydrolysis was Alcalase 2.4 L, 1% enzyme concentration, 5% suspension concentration for 4 hr. $IC_{50}$ value of ACE inhibitory activity of soybean protein isolate hydrolysate was $79.94 {\mu}g/mL$. These results suggest that soybean isolate protein hydrolysate from Alcalase 2.4 L may be of benefit for developing antihypertensive therapeutics.

Detection and Extraction Condition of Physiological Functional Compounds from Bran of Heugjinju rice (Oryza sativa L.) (흑진주벼 미강으로부터 생리기능성 물질의 탐색 및 추출조건)

  • 이국영;김재호;손종록;이종수
    • Food Science and Preservation
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    • v.8 no.3
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    • pp.296-301
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    • 2001
  • Physiological functionalities in various extracts of Heugjinju rice bran were determined and its optimal extraction condition were also investigated Angiotensin-converting enzyme(ACE) inhibitory activity, fibrinolytic activity and tyrosinase inhibitory activity were higher in water extracts than those of 80% ethanol and methanol, hexane. Electron donating abilities were 97.8% in hexane extract and 83% in water extracts. ACE inhibitor was maximally extracted from Heugjinju rice bran when it was treated with 20 times of distilled water for 12 h at 20 $\^{C}$. Fibrinolytic compound was also maximally extracted by treatment of 10 times of distilled water for 18 h at 20 $\^{C}$. Electron donating compound and tyrosinase inhibitor were maximally extracted by treatment of 20 times of hexane and 10 times of distilled water at 20 $\^{C}$ for 18 h, respectively

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Biological Activities of Fermented Dioscorea batatas Dence by two Stage Fermentation (2단 발효에 의한 발효마의 생리활성)

  • Jeon, Chun-Pyo;Lee, Joon-Geol;Lee, Jung-Bok;Park, Se-Cheol;Choi, Chung-Sig;Kim, Jang-Eok;Kwon, Gi-Seok
    • Korean Journal of Microbiology
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    • v.48 no.1
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    • pp.29-36
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    • 2012
  • This study was conducted to investigate antioxidative and physiological activities of two stage fermented Chinese Yam (TSFCY) by Monascus sp. MK2 and Lactobacillus brevis HLJ59. The extracts from TSFCY were measured to examine pigments, monacolin K contents, total polyphenol and flavonoid contents, DPPH radical scavenging activity, reducing power, ACE inhibitory activity and GABA contents. In this study, the results show that Monascus sp. MK2 and Lactobacillus brevis HLJ59, with Dioscorea batatas Dence. As the substrate can produce pigments (yellow, orange and red), monacolin K contents, total polyphenol and flavonoid contents, DPPH radical scavenging activity, reducing power, ACE inhibitory activity, and GABA contents at 14.03 (yellow), 13.88 (orange), 15.71 (red), 487.9 (MK, mg/kg), 723.8 (TP, mg/kg), 326.4 (TF, mg/kg), 81.7 (DPPH, %), and 1.5 (RP, O.D), respectively. In addition, the showed ACE inhibitory activity and GABA contents was 86.9% and 977.4 mg/kg in EtOH extract, respectively.

Physiological Activities of Hot Water Extract from Pine Bud (Pinus densiflora) (솔순 열수 추출물의 생리활성)

  • Cho, Eun-Kyung;Jeong, Bo-Rim;Choi, Young-Ju
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.11
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    • pp.1573-1579
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    • 2010
  • This research was performed to determine the antioxidant activity, nitrite scavenging activity, and its inhibitory activity on angiotensin converting enzyme (ACE), xanthine oxidase, $\alpha$-glucosidase, and elastase of hot water extract from pine bud (WPB). Antioxidant activity of WPB was measured by 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and superoxide dismutase (SOD)-like activity. DPPH radical scavenging activity and SOD-like activity of WPB were remarkably increased in a dose-dependent manner, and were about 71.4 and 85.4% at 2 mg/mL, respectively. The xanthine oxidase and ACE inhibitory activities were about 70.9 and 51.9% at 2 mg/mL of WPB, respectively. Nitrite scavenging activity of WPB was about 59.1, 53.8, and 39.5% on pH 1.2, 3.0, and 6.0 at 2 mg/mL, respectively. The WPB also showed elastase and $\alpha$-glucosidase inhibitory effects. These results revealed that pine bud have strong antioxidant activity and positive effects on the inhibition of xanthine oxidase, ACE, and elastase.

Cardiovascular Biofunctional Activity and Antioxidant Activity of Gugija (Lycium chinensis Mill) Species and Its Hybrids (구기자 품종과 교배종의 부위별 심혈관관련 질환 예방 기능성 및 항산화 활성비교)

  • Park, Won-Jong;Lee, Bong-Chun;Lee, Ju-Chan;Lee, Eun-Na;Song, Jung-Eun;Lee, Dae-Hyung;Lee, Jong-Soo
    • Korean Journal of Medicinal Crop Science
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    • v.15 no.6
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    • pp.391-397
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    • 2007
  • To develop new high valuable Gugija (Lycium chinensis), biofunctionalities of Gugija standard species and its hybrids were investigated and compared with each water extracts and methanol extracts from Lycii Fructus, Lycii Folium and buds and Lycii Cortex Radicis. Among various biofunctionalities of Gugija standard species, antioxidant activity was showed the highest in methanol extracts from buds of Cheongwoon species (93%) and antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity was 84.1% in the water extracts from Lycii Cortex Radicis of Cheongyang NO.7. Futhermore, methanol extracts from Lycii Cortex Radicis of Myungan A-2 hybrid showed 93.1% of antioxidant activity and 96.9% of ACE inhibitory activity was also showed in the methanol extracts from Lycii Fructus of DO148-72(A11) hybrid. However, fibrinolytic activity and anticholesteromia HMG-CoA reductase inhibitory activity were weak or not detected in almost of Gugija standard species and its hybrids. Therefore, we finally selected Cheongwoon Gugija standard species (buds) and Myungan A-2 hybrid (Lycii Cortex Radicis) as good antioxidant sources and also DO148-72 (A11) hybrid (Lycii Fructus) as excellent antihypertensive ACE inhibitior sources for manufacturing functional food product.

Antidiabetes and Angiotensin Converting Enzyme Inhibitory Activity of Sonchus asper (L) Hill Extract (큰방가지똥 추출물의 항당뇨 및 항고혈압효과)

  • Xu, Ming-Lu;Wang, Lan;Xu, Gui-Fang;Wang, Myeong-Hyeon
    • Korean Journal of Pharmacognosy
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    • v.42 no.1
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    • pp.61-67
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    • 2011
  • In this study, we evaluated the bioactivities of methanol extract and its solvent fractions of Sonchus asper (L.) Hill. The EtOAc fraction of S. asper exhibited more strong antioxidant activity than other extracts as evidenced by the strongest 1,1-diphenyl-2-picryl hydrazyl (DPPH) radical scavenging activity with a $EC_{50}$ value at $33.55\;{\mu}g/mL$ and reducing power, the total polyphenol (180.71 mg GAE/g) and flavonoid contents (145.86 mg QE/g) of S. asper extract were higher than other extracts. The EtOAc fraction of the S. asper also showed 47.38% mushroom tyrosinase inhibition activity, 56.22% ${\alpha}$-glucosidase inhibition and 46.58% ${\alpha}$-amylase inhibition ratio at 1 mg/mL. Both methylene chloride and EtOAc fractions of methanol extract of S. asper effectively reduced of the 86.34% and 62.03% angiotensin I converting enzyme (ACE) activity at 2 mg/mL, respectively. These findings suggest that the EtOAc fraction of the S. asper could be a potential antioxidant in food additive, medicinal, and industry product.

Development of effective heparin extraction method from pig by-products and analysis of their bioavailability

  • Lee, Da Young;Lee, Seung Yun;Kang, Hea Jin;Park, Yeonhwa;Hur, Sun Jin
    • Journal of Animal Science and Technology
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    • v.62 no.6
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    • pp.933-947
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    • 2020
  • This study was conducted to develop an effective heparin extraction method by using low-cost and highly effective enzymes from six pig by-products (liver, lung, heart, stomach, small intestine, and large intestine), and analyze their bioavailability. Low-cost and highly effective enzymes (alkaline-AK and papain) and a common enzyme (trypsin) were used for the heparin extraction. The angiotensin I- converting enzyme (ACE) inhibitory activity and the antimicrobial activity of extracted heparin were analyzed to verify their bioavailability. The average amount of heparin extracted per kilogram of pig by-products was 439 mg from the liver, 127 mg from the lung, 398 mg from the heart, 261 mg from the stomach, 197 mg from the small intestine, and 239 mg from the large intestine. Various enzymes were used to extract heparin, and the amount of extracted heparin was similar. Based on 1 g of pig by-product, the enzymes trypsin, papain, and alkaline-AK could extract 1,718 mg, 1,697 mg, and 1,905 mg of heparin, respectively. Heparin extracted from pig by-products showed antihypertensive activity and antimicrobial activity against Staphylococcus aureus at low populations. These results indicated that heparin can be obtained from pig by-products at a low cost.

Partial Purification of Mussel Adhesive Protein for Mytilus Edulis and Preparation of Mussel Protein Hydrolysates

  • Sun, Nam-Kyu;Song, Kyung-Bin
    • Preventive Nutrition and Food Science
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    • v.5 no.3
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    • pp.148-152
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    • 2000
  • Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.

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